The DOI matches its Crossref record; 99 of the 101 references it cites were found in a registry or an index.
Identification of Protein Interactions Involved in Cellular Signaling
Open accessAbstract
Protein-protein interactions drive biological processes. They are critical for all intra- and extracellular functions, and the technologies to analyze them are widely applied throughout the various fields of biological sciences. This study takes an in-depth view of some common principles of cellular regulation and provides a detailed account of approaches required to comprehensively map signaling protein-protein interactions in any particular cellular system or condition. We provide a critical review of the benefits and disadvantages of the yeast two-hybrid method and affinity purification coupled with mass spectrometric procedures for identification of signaling protein-protein interactions. In particular, we emphasize the quantitative and qualitative differences between tandem affinity and one-step purification (such as FLAG and Strep tag) methods. Although applicable to all types of interaction studies, a special section is devoted in this review to aspects that should be considered when attempting to identify signaling protein interactions that often are transient and weak by nature. Finally, we discuss shotgun and quantitative information that can be gleaned by MS-coupled methods for analysis of multiprotein complexes.
Overview
Integrity signals
Registry
Cites
Statistics
Verification
Claims the paper makes
Claims other papers make about this one
Each is checked against this paper’s own text: does it say what the citing paper says it does?
In the citing paper
“suggesting that they may be functionally related69–71 or operate together72,73 to mediate phenotypic features associated with UDN-P9’s disease and hypomyelinating leukodystropy-20”
From Few shot learning for phenotype-driven diagnosis of patients with rare genetic diseases (2025) · cites this paper as [72]
Citations
Cites
Mass spectrometry-based proteomics
Aebersold, R., & Mann, M. (2003) · Nature · doi:10.1038/nature01511 · Cited by 6,955
A novel genetic system to detect protein–protein interactions
Fields, S., & Song, O.-K. (1989) · Nature · doi:10.1038/340245a0 · Cited by 6,152
Ong, S.-E., Blagoev, B., Kratchmarova, I., Kristensen, D. B., Steen, H., Pandey, A., & Mann, M. (2002) · Molecular & Cellular Proteomics · doi:10.1074/mcp.m200025-mcp200 · Cited by 5,574
Jaakkola, P., Mole, D. R., Tian, Y.-M., Wilson, M. I., Gielbert, J., Gaskell, S. J., Kriegsheim, A. V., Hebestreit, H. F., Mukherji, M., Schofield, C. J., et al. (2001) · Science · doi:10.1126/science.1059796 · Cited by 5,535
Functional organization of the yeast proteome by systematic analysis of protein complexes
Gavin, A., Böesche, M., Krause, R., Grandi, P., Marzioch, M., Bauer, A., Schultz, J., Rick, J. M., Michon, A., Cruciat, C., et al. (2002) · Nature · doi:10.1038/415141a · Cited by 4,729
A comprehensive analysis of protein–protein interactions in Saccharomyces cerevisiae
Uetz, P., Giot, L., Cagney, G., Mansfield, T. A., Judson, R. S., Knight, J. R., Lockshon, D., Narayan, V., Srinivasan, M., Pochart, P., et al. (2000) · Nature · doi:10.1038/35001009 · Cited by 4,706
Ross, P. L., Huang, Y. N., Marchese, J. N., Williamson, B., Parker, K., Hattan, S., Khainovski, N., Pillai, S., Dey, S., Daniels, S., et al. (2004) · Molecular & Cellular Proteomics · doi:10.1074/mcp.m400129-mcp200 · Cited by 4,401
Systematic identification of protein complexes in Saccharomyces cerevisiae by mass spectrometry
Ho, Y., Gruhler, A., Heilbut, A. M., Bader, G. D., Moore, L., Adams, S., Millar, A., Taylor, P. P., Bennett, K. L., Boutilier, K., et al. (2002) · Nature · doi:10.1038/415180a · Cited by 3,573
A comprehensive two-hybrid analysis to explore the yeast protein interactome
Ito, T., Chiba, T., Ozawa, R., Yoshida, M., Hattori, M., & Sakaki, Y. (2001) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.061034498 · Cited by 3,566
Global landscape of protein complexes in the yeast Saccharomyces cerevisiae
Krogan, N. J., Cagney, G., Yu, H., Zhong, G., Guo, X., Ignatchenko, A., Li, J., Pu, S., Datta, N., Tikuisis, A., et al. (2006) · Nature · doi:10.1038/nature04670 · Cited by 2,964
A generic protein purification method for protein complex characterization and proteome exploration
Rigaut, G., Shevchenko, A., Rutz, B., Wilm, M., Mann, M., & Séraphin, B. (1999) · Nature Biotechnology · doi:10.1038/13732 · Cited by 2,707
A Human Protein-Protein Interaction Network: A Resource for Annotating the Proteome
Stelzl, U., Worm, U., Lalowski, M. M., Haenig, C., Brembeck, F. H., Goehler, H., Strödicke, M., Zenkner, M., Schoenherr, A., Koeppen, S., et al. (2005) · Cell · doi:10.1016/j.cell.2005.08.029 · Cited by 2,433
Comparative assessment of large-scale data sets of protein–protein interactions
von Mering, C., Krause, R., Snel, ., Cornell, M. J., Oliver, S. G., Fields, S., & Peer Bork, B. (2002) · Nature · doi:10.1038/nature750 · Cited by 2,339
Reaching for high-hanging fruit in drug discovery at protein–protein interfaces
Wells, J. A., & McClendon, C. L. (2007) · Nature · doi:10.1038/nature06526 · Cited by 2,002
A Protein Interaction Map of Drosophila melanogaster
Giot, L., Bader, J. S., Brouwer, C., Chaudhuri, A., Kuang, B., Li, Y., Hao, Y. L., Ooi, C. E., Godwin, B., Vitols, E., et al. (2003) · Science · doi:10.1126/science.1090289 · Cited by 1,863
Quantitative mass spectrometry in proteomics: a critical review
Bantscheff, M., Schirle, M., Sweetman, G. M. A., Rick, J. M., & Küster, B. (2007) · Analytical and Bioanalytical Chemistry · doi:10.1007/s00216-007-1486-6 · Cited by 1,721
High-Quality Binary Protein Interaction Map of the Yeast Interactome Network
Yu, H., Braun, P., Yıldırım, M. A., Lemmens, I., Venkatesan, K., Sahalie, J., Hirozane-Kishikawa, T., Gebreab, F., Li, N., Simonis, N., et al. (2008) · Science · doi:10.1126/science.1158684 · Cited by 1,392
Wang, Y., Cortez, D., Yazdi, P., Neff, N., Elledge, S. J., & Qin, J. (2000) · Genes & Development · doi:10.1101/gad.14.8.927 · Cited by 1,221
A physical and functional map of the human TNF-α/NF-κB signal transduction pathway
Bouwmeester, T., Bauch, A., Ruffner, H., Angrand, P., Bergamini, G., Croughton, K., Cruciat, C., Eberhard, D., Gagneur, J., Ghidelli, S., et al. (2004) · Nature Cell Biology · doi:10.1038/ncb1086 · Cited by 1,030
Protein tagging and detection with engineered self-assembling fragments of green fluorescent protein
Cabantous, S., Terwilliger, T. C., & Waldo, G. S. (2004) · Nature Biotechnology · doi:10.1038/nbt1044 · Cited by 957
Quantitative Analysis of Hsp90-Client Interactions Reveals Principles of Substrate Recognition
Taipale, M., Krykbaeva, I., Koeva, M., Kayatekin, C., Westover, K. D., Karras, G. I., & Lindquist, S. (2012) · Cell · doi:10.1016/j.cell.2012.06.047 · Cited by 879
Post-translational modifications in signal integration
Deribe, Y. L., Pawson, T., & Dikic, I. (2010) · Nature Structural & Molecular Biology · doi:10.1038/nsmb.1842 · Cited by 876
AU Binding Proteins Recruit the Exosome to Degrade ARE-Containing mRNAs
Chen, C.-Y., Gherzi, R., Ong, S.-E., Chan, E. L., Raijmakers, R., Pruijn, G. J. M., Stoecklin, G., Moroni, C., Mann, M., & Karin, M. (2001) · Cell · doi:10.1016/s0092-8674(01)00578-5 · Cited by 865
Roberts, A. W., Seymour, J. F., Brown, J. R., Wierda, W. G., Kipps, T. J., Khaw, S. L., Carney, D. A., He, S., Huang, D. C. S., Xiong, H., et al. (2011) · Journal of Clinical Oncology · doi:10.1200/jco.2011.34.7898 · Cited by 855
SAINT: probabilistic scoring of affinity purification–mass spectrometry data
Choi, H., Larsen, B., Lin, Z.-Y., Breitkreutz, A., Mellacheruvu, D., Fermin, D., Qin, Z. S., Tyers, M., Gingras, A.-C., & Nesvizhskii, A. I. (2011) · Nature Methods · doi:10.1038/nmeth.1541 · Cited by 800
Protein–protein interactions define specificity in signal transductionPreprint
Pawson, T. J., & Nash, P. (2000) · Genes & Development · doi:10.1101/gad.14.9.1027 · Cited by 780
Analysis of protein complexes using mass spectrometry
Gingras, A., Gstaiger, M., Raught, B., & Aebersold, R. H. (2007) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm2208 · Cited by 727
High-Throughput Mapping of a Dynamic Signaling Network in Mammalian Cells
Barrios‐Rodiles, M., Brown, K. R., Ozdamar, B., Bose, R., Liu, Z., Donovan, R. S., Shinjo, F., Liu, Y., Dembowy, J., Taylor, I. W., et al. (2005) · Science · doi:10.1126/science.1105776 · Cited by 726
An atlas of combinatorial transcriptional regulation in mouse and man
Ravasi, T., Suzuki, H., Cannistraci, C. V., Katayama, S., Bajic, V. B., Tan, K., Akalin, A., Schmeier, S., Kanamori-Katayama, M., Bertin, N., et al. (2010) · Cell · doi:10.1016/j.cell.2010.01.044 · Cited by 715
A Global Protein Kinase and Phosphatase Interaction Network in Yeast
Breitkreutz, A., Choi, H., Sharom, J. R., Boucher, L., Neduva, V., Larsen, B. G., Lin, Z., Breitkreutz, B., Stark, C., Liu, G., et al. (2010) · Science · doi:10.1126/science.1176495 · Cited by 684
Temporal analysis of phosphotyrosine-dependent signaling networks by quantitative proteomics
Blagoev, B., Ong, S., Kratchmarova, I., & Mann, M. (2004) · Nature Biotechnology · doi:10.1038/nbt1005 · Cited by 681
CIP2A inhibits PP2A in human malignancies
Junttila, M. R., Puustinen, P., Niemelä, M., Ahola, R., Arnold, H., Böttzauw, T., Ala-aho, R., Nielsen, C., Ivaska, J., Taya, Y., et al. (2007) · Cell · doi:10.1016/j.cell.2007.04.044 · Cited by 677
Self-citationThe Strep-tag system for one-step purification and high-affinity detection or capturing of proteins
Schmidt, T. G. M., & Skerra, A. (2007) · Nature Protocols · doi:10.1038/nprot.2007.209 · Cited by 635
Štagljar, I., Korostensky, C., Johnsson, N., & Heesen, S. T. (1998) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.95.9.5187 · Cited by 596
Trinkle‐Mulcahy, L., Boulon, S., Lam, Y. W., Urcia, R., Boisvert, F., Vandermoere, F., MORRICE, N. A., Swift, S., Rothbauer, U., Leonhardt, H., et al. (2008) · The Journal of Cell Biology · doi:10.1083/jcb.200805092 · Cited by 453
Visualization of molecular interactions by fluorescence complementation
Kerppola, T. K. (2006) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm1929 · Cited by 430
Rac–MEKK3–MKK3 scaffolding for p38 MAPK activation during hyperosmotic shock
Uhlik, M. T., Abell, A. N., Johnson, N. L., Sun, W., Cuevas, B. D., Lobel-Rice, K. E., Horne, E. A., Dell’Acqua, M. L., & Johnson, G. L. (2003) · Nature Cell Biology · doi:10.1038/ncb1071 · Cited by 378
Herzog, F., Kahraman, A., Boehringer, D., Mak, R., Bracher, A., Walzthoeni, T., Leitner, A., Beck, M., Hartl, F. U., Ban, N., et al. (2012) · Science · doi:10.1126/science.1221483 · Cited by 372
Goudreault, M., D'Ambrosio, L. M., Kean, M. J., Mullin, M. J., Larsen, B. G., Sanchez, A., Chaudhry, S., Chen, G. I., Sicheri, F., Nesvizhskii, A. I., et al. (2009) · Molecular & Cellular Proteomics · doi:10.1074/mcp.m800266-mcp200 · Cited by 359
Multiple pathways regulated by the tumor suppressor PP2A in transformation
Westermarck, J., & Hahn, W. C. (2008) · Trends in Molecular Medicine · doi:10.1016/j.molmed.2008.02.001 · Cited by 344
Self-citationIntegrated network analysis platform for protein-protein interactions
Wu, J., Vallenius, T., Ovaska, K., Westermarck, J. K., Mäkelä, T. P., & Hautaniemi, S. (2008) · Nature Methods · doi:10.1038/nmeth.1282 · Cited by 320
Self-citationThe nucleoskeleton as a genome-associated dynamic 'network of networks'
Simon, D. N., & Wilson, K. L. (2011) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm3207 · Cited by 282
Structural basis of 14-3-3 protein functions
Obšil, T., & Obšilová, V. (2011) · Seminars in Cell and Developmental Biology · doi:10.1016/j.semcdb.2011.09.001 · Cited by 275
Designing customized cell signalling circuits
Lim, W. A. (2010) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm2904 · Cited by 257
An integrated workflow for charting the human interaction proteome: insights into the PP2A system
Glatter, T., Wepf, A., Aebersold, R. H., & Gstaiger, M. (2009) · Molecular Systems Biology · doi:10.1038/msb.2008.75 · Cited by 257
IQGAP1 Is a Scaffold for Mitogen-Activated Protein Kinase Signaling
Roy, M., Li, Z., & Sacks, D. B. (2005) · Molecular and Cellular Biology · doi:10.1128/mcb.25.18.7940-7952.2005 · Cited by 248
Cellular stress and nucleolar function
Mayer, C., & Grummt, I. (2005) · Cell Cycle · doi:10.4161/cc.4.8.1925 · Cited by 233
Identification of protein‐protein interactions using in vivo cross‐linking and mass spectrometry
Vasilescu, J., Guo, X., & Kast, J. (2004) · PROTEOMICS · doi:10.1002/pmic.200400856 · Cited by 226
Crosslinking combined with mass spectrometry for structural proteomics
Petrotchenko, E. V., & Borchers, C. H. (2010) · Mass Spectrometry Reviews · doi:10.1002/mas.20293 · Cited by 208
MYC-Dependent Regulation and Prognostic Role of CIP2A in Gastric Cancer
Khanna, A., Böckelman, C., Hemmes, A., Junttila, M. R., Wiksten, J.-P., Lundin, M., Junnila, S., Murphy, D. J., Evan, G. I., Haglund, C., et al. (2009) · JNCI: Journal of the National Cancer Institute · doi:10.1093/jnci/djp103 · Cited by 185
Self-citationAnalyzing Protein‐Protein Interactions from Affinity Purification‐Mass Spectrometry Data with SAINT
Choi, H., Liu, G., Mellacheruvu, D., Tyers, M., Gingras, A., & Nesvizhskii, A. I. (2012) · Current Protocols in Bioinformatics · doi:10.1002/0471250953.bi0815s39 · Cited by 168
Rinner, O., Mueller, L. N., Hubálek, M., Müller, M., Gstaiger, M., & Aebersold, R. H. (2007) · Nature Biotechnology · doi:10.1038/nbt1289 · Cited by 165
Scaffolds: interaction platforms for cellular signalling circuits
Zeke, A., Lukács, M., Lim, W. A., & Reményi, A. (2009) · Trends in Cell Biology · doi:10.1016/j.tcb.2009.05.007 · Cited by 158
Assembly of ribosomes and spliceosomes: complex ribonucleoprotein machines
Staley, J. P., & Woolford, J. L. (2009) · Current Opinion in Cell Biology · doi:10.1016/j.ceb.2009.01.003 · Cited by 157
CIP2A mediates effects of bortezomib on phospho-Akt and apoptosis in hepatocellular carcinoma cells
Chen, K.-F., Liu, C.-Y., Lin, Y.-C., Yu, H.-C., Liu, T.-H., Hou, D.-R., Chen, P.-J., & Cheng, A.-L. (2010) · Oncogene · doi:10.1038/onc.2010.357 · Cited by 155
Reményi, A., Good, M. C., Bhattacharyya, R. P., & Lim, W. A. (2005) · Molecular Cell · doi:10.1016/j.molcel.2005.10.030 · Cited by 154
Targeting the SH2-Kinase Interface in Bcr-Abl Inhibits Leukemogenesis
Grebien, F., Hantschel, O. D., Wojcik, J. B., Kaupe, I., Kovačic, B., Wyrzucki, A. M., Gish, G. D., Cerny‐Reiterer, S., Koide, A., Beug, H., et al. (2011) · Cell · doi:10.1016/j.cell.2011.08.046 · Cited by 152
Two-hybrid technologies in proteomics research
Suter, B., Kittanakom, S., & Štagljar, I. (2008) · Current Opinion in Biotechnology · doi:10.1016/j.copbio.2008.06.005 · Cited by 140
Lucas, C. M., Harris, R. J., Giannoudis, A., Copland, M., Slupsky, J. R., & Clark, R. E. (2011) · Blood · doi:10.1182/blood-2010-08-304477 · Cited by 138
Probing the Molecular Environment of Membrane Proteins In Vivo
Wittke, S., Lewke, N., Müller, S., & Johnsson, N. (1999) · Molecular Biology of the Cell · doi:10.1091/mbc.10.8.2519 · Cited by 136
Kusumi, A., Fujiwara, T. K., Morone, N., Yoshida, K. J., Chadda, R., Xie, M., Kasai, R. S., & Suzuki, K. G. N. (2012) · Seminars in Cell and Developmental Biology · doi:10.1016/j.semcdb.2012.01.018 · Cited by 135
Mapping multiprotein complexes by affinity purification and mass spectrometry
Collins, M. O., & Choudhary, J. S. (2008) · Current Opinion in Biotechnology · doi:10.1016/j.copbio.2008.06.002 · Cited by 125
Recent advances in charting protein–protein interaction: mass spectrometry-based approaches
Gavin, A., Maeda, K., & Kühner, S. (2010) · Current Opinion in Biotechnology · doi:10.1016/j.copbio.2010.09.007 · Cited by 124
Junttila, M. R., Saarinen, S., Schmidt, T. G. M., Kast, J., & Westermarck, J. K. (2005) · PROTEOMICS · doi:10.1002/pmic.200400991 · Cited by 122
Self-citationSmall Molecule Inhibitors of Protein–Protein Interactions
Roberts, G. C. K. (2012) · Springer eBooks · doi:10.1007/978-3-642-16712-6_100964 · Cited by 118
The DEXD/H‐box RNA helicase RHII/Gu is a co‐factor for c‐Jun‐activated transcription
Westermarck, J. K., Weiß, C., Saffrich, R., Kast, J., Musti, A. M., Wessely, M., Ansorge, W. J., Séraphin, B., Wilm, M. S., Valdez, B. C., et al. (2002) · The EMBO Journal · doi:10.1093/emboj/21.3.451 · Cited by 114
Self-citationProtein–Protein Interaction Panel Using Mouse Full-Length cDNAsPreprint
Suzuki, H., Fukunishi, Y., Kagawa, I., Saito, R., Oda, H., Endo, T., Kondo, S., Bono, H. U., Okazaki, Y., & Hayashizaki, Y. (2001) · Genome Research · doi:10.1101/gr.180101 · Cited by 109
Johansen, L. D., Naumanen, T., Karnoe, A., Westerlund, N., Gromova, I., Junttila, M. R., Nielsen, C. W., Bøttzauw, T., Tolkovsky, A. M., Westermarck, J. K., et al. (2008) · Journal of Cell Science · doi:10.1242/jcs.013722 · Cited by 104
Self-citationQuantitative Proteomic Analysis of Protein Complexes
Pflieger, D., Jünger, M. A., Müller, M., Rinner, O., Lee, H., Gehrig, P., Gstaiger, M., & Aebersold, R. H. (2007) · Molecular & Cellular Proteomics · doi:10.1074/mcp.m700282-mcp200 · Cited by 103
Xu, X., Song, Y., Li, Y., Chang, J., zhang, H., & An, L. (2010) · Protein Expression and Purification · doi:10.1016/j.pep.2010.04.009 · Cited by 101
Mapping protein–protein interactions by mass spectrometry
Vasilescu, J., & Figeys, D. (2006) · Current Opinion in Biotechnology · doi:10.1016/j.copbio.2006.06.008 · Cited by 81
Niemelä, M., Kauko, O., Sihto, H., Mpindi, J.-P., Nicorici, D., Pernilä, P., Kallioniemi, O.-P., Joensuu, H., Hautaniemi, S., & Westermarck, J. (2012) · Oncogene · doi:10.1038/onc.2011.599 · Cited by 79
Self-citationSmolka, M. B., de Albuquerque, C. P., Chen, S., Schmidt, K. H., Wei, X. X., Kolodner, R. D., & Zhou, H. (2005) · Molecular & Cellular Proteomics · doi:10.1074/mcp.m500115-mcp200 · Cited by 78
Chang, I. (2006) · PROTEOMICS · doi:10.1002/pmic.200600225 · Cited by 76
Hannan, K. M., Thomas, G., & Pearson, R. B. (2003) · Biochemical Journal · doi:10.1042/bj20021709 · Cited by 74
Skarra, D. V., Goudreault, M., Choi, H., Mullin, M. J., Nesvizhskii, A. I., Gingras, A., & Honkanen, R. E. (2011) · PROTEOMICS · doi:10.1002/pmic.201000770 · Cited by 73
Advancing formaldehyde cross-linking towards quantitative proteomic applications
Klockenbusch, C., O’Hara, J. E., & Kast, J. (2012) · Analytical and Bioanalytical Chemistry · doi:10.1007/s00216-012-6065-9 · Cited by 68
Fashena, S. J., Serebriiskii, I. G., & Golemis, E. A. (2000) · Gene · doi:10.1016/s0378-1119(00)00182-7 · Cited by 67
RING Finger E3 Ubiquitin Ligases: Structure and Drug Discovery
Chasapis, C. T., & Spyroulias, G. A. (2009) · Current Pharmaceutical Design · doi:10.2174/138161209789271825 · Cited by 65
Morell, M., Espargaró, A., Avilés, F. X., & Ventura, S. (2007) · Nature Protocols · doi:10.1038/nprot.2007.496 · Cited by 64
Mammalian two-hybrids come of age
Lievens, S., Lemmens, I. H., & Tavernier, J. H. (2009) · Trends in Biochemical Sciences · doi:10.1016/j.tibs.2009.06.009 · Cited by 61
Raf-1 activation disrupts its binding to keratins during cell stress
Ku, N., Fu, H., & Omary, M. B. (2004) · The Journal of Cell Biology · doi:10.1083/jcb.200402051 · Cited by 57
Mialon, A., Sankinen, M., Söderström, H., Junttila, T. T., Holmström, T. H., Koivusalo, R., Papageorgiou, A. C., Johnson, R. S., Hietanen, S., Elenius, K., et al. (2005) · Molecular and Cellular Biology · doi:10.1128/mcb.25.12.5040-5051.2005 · Cited by 55
Self-citationDetection of altered protein conformations in living cells
Raquet, X., Eckert, J. H., Müller, S., & Johnsson, N. (2001) · Journal of Molecular Biology · doi:10.1006/jmbi.2000.4239 · Cited by 45
From protein interaction networks to novel therapeutic strategies
Jaeger, S., & Aloy, P. (2012) · IUBMB Life · doi:10.1002/iub.1040 · Cited by 44
Mathiasen, D. P., Egebjerg, C., Andersen, S. H., Rafn, B., Puustinen, P., Khanna, A., Daugaard, M., Valo, E., Tuomela, S., Bøttzauw, T., et al. (2012) · Oncogene · doi:10.1038/onc.2011.230 · Cited by 44
Self-citationDrug target deconvolution by chemical proteomics
Raida, M. (2011) · Current Opinion in Chemical Biology · doi:10.1016/j.cbpa.2011.06.016 · Cited by 43
Regulation of p14ARF Through Subnuclear Compartmentalization
Gjerset, R. A., & Bandyopadhyay, K. (2006) · Cell Cycle · doi:10.4161/cc.5.7.2623 · Cited by 43
Kim, J. H., Xu, E. Y., Sacks, D. B., Lee, J. H., Shu, L., Xia, B., & Kong, A. T. (2012) · Antioxidants and Redox Signaling · doi:10.1089/ars.2012.4586 · Cited by 42
Small-Molecule Inhibitors of Protein–Protein Interactions
Berg, T. (2010) · IMPERIAL COLLEGE PRESS eBooks · doi:10.1142/9781848163409_0012 · Cited by 39
Interactive learning: Lessons from two hybrids over two decades
Fields, S. (2009) · PROTEOMICS · doi:10.1002/pmic.200900236 · Cited by 39
[Drug target deconvolution by chemical proteomics].
Gong, L., & Kang, J. (2020) · PubMed · doi:10.3724/sp.j.1123.2019.12014 · Cited by 38
Mdm2 associates with Ras effector NORE1 to induce the degradation of oncoprotein HIPK1
Lee, D., Park, S., Sung, K. S., Park, J., Lee, S. B., Park, S., Lee, H., Ahn, J., Choi, S. J., Lee, S., et al. (2011) · EMBO Reports · doi:10.1038/embor.2011.235 · Cited by 31
Belozerov, V. E., Lin, Z., Gingras, A., McDermott, J. C., & Siu, K. W. M. (2012) · Molecular and Cellular Biology · doi:10.1128/mcb.00232-12 · Cited by 27
Nucleolar AATF regulates c-Jun–mediated apoptosis
Ferraris, S. E., Isoniemi, K. O., Torvaldson, E., Anckar, J., Westermarck, J. K., & Eriksson, J. (2012) · Molecular Biology of the Cell · doi:10.1091/mbc.e12-05-0419 · Cited by 27
Self-citationAnalysis of protein-protein proximities using the split-ubiquitin system
Lehming, N. (2002) · Briefings in Functional Genomics and Proteomics · doi:10.1093/bfgp/1.3.230 · Cited by 23
Dolgin, E. (2012) · Nature Medicine · doi:10.1038/nm0512-642 · Cited by 20
Chemical proteomics and its impact on the drug discovery process
Miao, Q., Zhang, C., & Kast, J. (2012) · Expert Review of Proteomics · doi:10.1586/epr.12.22 · Cited by 15
Chemical Proteomics in Drug Discovery
Drewes, G. (2011) · Methods in molecular biology · doi:10.1007/978-1-61779-364-6_2 · Cited by 9
Cited by
Sorted by citations
The Critical Node Detection Problem in networks: A survey
Lalou, M., Tahraoui, M. A., & Kheddouci, H. (2018) · Computer Science Review · doi:10.1016/j.cosrev.2018.02.002 · Cited by 328
Egea, J., Fabregat, I., Frapart, Y., Ghezzi, P., Görlach, A., Kietzmann, T., Kubaichuk, K. I., Knaus, U. G., López, M. G., González, G. O., et al. (2017) · Redox Biology · doi:10.1016/j.redox.2017.05.007 · Cited by 321
Trans-Omics: How To Reconstruct Biochemical Networks Across Multiple ‘Omic’ Layers
Yugi, K., Kubota, H., Hatano, A., & Kuroda, S. (2016) · Trends in Biotechnology · doi:10.1016/j.tibtech.2015.12.013 · Cited by 258
Morris, J. H., Knudsen, G. M., Verschueren, E., Johnson, J. R., Cimermančič, P., Greninger, A. L., & Pico, A. R. (2014) · Nature Protocols · doi:10.1038/nprot.2014.164 · Cited by 210
Systematic Targeting of Protein–Protein Interactions
Modell, A. E., Blosser, S. L., & Arora, P. S. (2016) · Trends in Pharmacological Sciences · doi:10.1016/j.tips.2016.05.008 · Cited by 184
Metadata
- Authors
- Westermarck, J., Ivaska, J., & Corthals, G. L.
- Affiliations
- Åbo Akademi University (FI)
- Corresponding author
- Corthals, Garry L.
- Venue
- Molecular & Cellular Proteomics
- Publisher
- Elsevier BV
- Published
- 2013-07
- Volume
- 12
- Issue
- 7
- Pages
- 1752-1763
- ISSN
- 1535-9476 (ISSN-L)
- PMC
- PMC3708163
- OpenAlex
- W2147130215
- Cited by
- 143
- References
- 101
- Citations by year
- 2026: 21 · 2025: 19 · 2024: 15 · 2023: 8 · 2022: 13 · 2021: 12 · 2020: 8 · 2019: 12 · 2018: 7 · 2017: 5 · 2016: 7 · 2015: 4 · 2014: 9 · 2013: 1
- FWCI
- 0.66
- Type
- journal article
- Language
- en
- Open access
- hybrid
- doi.org
- Licence
- Locations
- Molecular & Cellular Proteomics (publishedVersion, cc-by)
- PubMed Central (publishedVersion)
- PubMed (publishedVersion)
- Topics
- Physical Sciences › Chemistry › Spectroscopy › Advanced Proteomics Techniques and Applications
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Bioinformatics and Genomic Networks
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Cell Biology › Biotin and Related Studies
- Keywords
- protein-protein interaction, signal transduction, yeast two-hybrid, affinity purification, tandem affinity purification, FLAG tag, Strep-tag, protein complexes, protein interaction mapping
- MeSH terms
- Humans, Mass Spectrometry, Signal Transduction, Two-Hybrid System Techniques, Protein Interaction Mapping
About these checks
Registry, retraction, Cites and statistics results are computed, not judged, with one exception: a printed reference that no index lists is read once by a model before it counts as a citation error. Claims are extracted by a model and kept only when their quote appears verbatim in the text; each cited source is then checked, with a model’s help, for whether it says what the claim relies on. Those verdicts can be wrong — read the claim’s quote and the cited source before relying on one.
Statistics and arithmetic are recomputed, not judged.
Confidence bands are shown only for fields calibrated on our annotated test set. None is calibrated yet, so no band is shown.
What counts as a claim ›How we measure confidence ›How we check this ›
Are you an author, or do you see a problem with this page? Request a review